This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Moenomycin A (MmA) is the natural product that inhibits bacterial cell wall biosynthesis by binding to the peptidoglycan glycosyltransferases (PGTs), the enzymes that make the glycan chains of peptidoglycan. MmA is remarkably potent, but its clinical utility has been hampered by its poor physicochemical properties. A better understanding of the roles of particular structural features in enzyme inhibition may ultimately enable the design of moenomycin analogs with improved properties.